Targeting Capacity and Conservation of PreP Homologues Localization in Mitochondria of Different Species

被引:39
作者
Alikhani, Nyosha [1 ]
Berglund, Anna-Karin [1 ]
Engmann, Tanja [2 ]
Spanning, Erika [1 ]
Voegtle, F. -Nora [3 ,4 ]
Pavlov, Pavel [1 ]
Meisinger, Chris [3 ,5 ]
Langer, Thomas [2 ,6 ]
Glaser, Elzbieta [1 ]
机构
[1] Stockholm Univ, Dept Biochem & Biophys, Arrhenius Labs Nat Sci, SE-10691 Stockholm, Sweden
[2] Univ Cologne, Inst Genet, Ctr Mol Med, D-50674 Cologne, Germany
[3] Univ Freiburg, Inst Biochem & Mol Biol, ZBMZ, D-79104 Freiburg, Germany
[4] Univ Freiburg, Fak Biol, D-79104 Freiburg, Germany
[5] Univ Freiburg, BIOSS, Ctr Biol Signalling Studies, D-79104 Freiburg, Germany
[6] Max Planck Inst Biol Aging, D-50931 Cologne, Germany
基金
瑞典研究理事会; 欧洲研究理事会;
关键词
mitochondrial import; presequence; PreP; Cym1/Mop112; peptide degradation; PROTEIN IMPORT; INTERMEMBRANE SPACE; TOM COMPLEX; SACCHAROMYCES-CEREVISIAE; PROCESSING PEPTIDASE; PLANT MITOCHONDRIAL; APOCYTOCHROME-C; OUTER-MEMBRANE; TRANSLOCATION; PRESEQUENCES;
D O I
10.1016/j.jmb.2011.05.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mitochondrial presequences and other unstructured peptides are degraded inside mitochondria by presequence proteases (PrePs) identified in Arabidopsis thaliana (AtPreP), humans (hPreP), and yeast (Cym1/Mop112). The presequences of A. thaliana and human PreP are predicted to consist of 85 and 29 amino acids, respectively, whereas the Saccharomyces cerevisiae Cym1/Mop112 presequence contains only 7 residues. These differences may explain the reported targeting of homologous proteins to different mitochondrial subcompartments. Here we have investigated the targeting capacity of the PreP homologues' presequences. We have produced fusion constructs containing N-terminal portions of AtPreP(1-125), hPreP(1-69), and Cym1(1-40) coupled to green fluorescent protein (GFP) and studied their import into isolated plant, mammalian, and yeast mitochondria, followed by mitochondrial subfractionation. Whereas the AtPreP presequence has the capacity to target GFP into the mitochondrial matrix of all three species, the hPreP presequence only targets GFP to the matrix of mammalian and yeast mitochondria. The Cym1/Mop112 presequence has an overall much weaker targeting capacity and only ensures mitochondrial sorting in its host species yeast. Revisiting the submitochondrial localization of Cym1 revealed that endogenous Cym1/Mop112 is localized to the matrix space, as has been previously reported for the plant and human homologues. Moreover, complementation studies in yeast show that native AtPreP restores the growth phenotype of yeast cells lacking Cym1, demonstrating functional conservation. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:400 / 410
页数:11
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